1XXN
Crystal structure of a mesophilic xylanase A from Bacillus subtilis 1A1
Summary for 1XXN
| Entry DOI | 10.2210/pdb1xxn/pdb |
| Descriptor | Endo-1,4-beta-xylanase A, S,R MESO-TARTARIC ACID (3 entities in total) |
| Functional Keywords | family 11 xylanase, thermostability, hydrolase |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 1 |
| Total formula weight | 20545.07 |
| Authors | Murakami, M.T.,Ruller, R.,Ward, R.J.,Arni, R.K. (deposition date: 2004-11-07, release date: 2005-10-18, Last modification date: 2023-08-23) |
| Primary citation | Murakami, M.T.,Arni, R.K.,Vieira, D.S.,Degreve, L.,Ruller, R.,Ward, R.J. Correlation of temperature induced conformation change with optimum catalytic activity in the recombinant G/11 xylanase A from Bacillus subtilis strain 168 (1A1). Febs Lett., 579:6505-6510, 2005 Cited by PubMed Abstract: The 1.7A resolution crystal structure of recombinant family G/11 beta-1,4-xylanase (rXynA) from Bacillus subtilis 1A1 shows a jellyroll fold in which two curved beta-sheets form the active-site and substrate-binding cleft. The onset of thermal denaturation of rXynA occurs at 328 K, in excellent agreement with the optimum catalytic temperature. Molecular dynamics simulations at temperatures of 298-328 K demonstrate that below the optimum temperature the thumb loop and palm domain adopt a closed conformation. However, at 328 K these two domains separate facilitating substrate access to the active-site pocket, thereby accounting for the optimum catalytic temperature of the rXynA. PubMed: 16289057DOI: 10.1016/j.febslet.2005.10.039 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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